The interaction of a series of metal derivatives of 5, 10, 15, 20-tetrakis(4-sulfonato-phenyl)porphyrin (MTPPS4, M = Cu(II), Pt(II), Ni(II), Zn(II) and Co(II)), including the metal free porphyrin (TPPS4), with the aromatic amino acids L-tryptophan (L-Trp), L-and D-phenylalanine (L-and D-Phe) and L-histidine (L-His) have been investigated through UV/Vis spectroscopy. The amino acid L-serine (L-Ser) has been included as reference compound. The spectroscopic changes induced by adding the amino acids have been exploited to evaluate the extent of interaction between the molecular components in the supramolecular adducts. The binding constants have been estimated for most of the investigated systems, assuming a simple 1:1 equilibrium. The bathochromic shifts of the B-bands, the extent of hypochromicity and the binding constants have been analyzed through two chemical descriptors. All the data point to the important role played by the steric hindrance introduced by axial ligands coordinated to the metal ions and to the degree of hydrophobicity and size of the aromatic moiety in the amino acids.
Keywords: amino acids; hydrophobicity; porphyrins; supramolecular adducts.